Protein kinase C inactivation by Fenton's-reaction at discrete CU++ binding sites
| Autor: | Nicola Traverso, Cinzia Domenicotti, Damiano Cottalasso, Umberto M. Marinari, Roberta Ricciarelli, Stefano Menini, M.Adelaide Pronzato |
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| Rok vydání: | 1996 |
| Předmět: |
inorganic chemicals
Male benzoate hydroxylation copper ions fenton's reaction free radicals metal binding sites protein kinase c tryptophan fluorescence Iron Clinical Biochemistry Kinetics Immunoblotting chemistry.chemical_element Iron Chelating Agents Biochemistry chemistry.chemical_compound Genetics Animals Binding site Rats Wistar Hydrogen peroxide Molecular Biology Protein kinase C Protein Kinase C chemistry.chemical_classification Binding Sites Hydroxyl Radical Cell Biology Hydrogen Peroxide Pentetic Acid Copper Rats Enzyme chemistry Liver Reagent Biophysics Hydroxyl radical |
| Zdroj: | Europe PubMed Central |
| ISSN: | 1039-9712 |
| Popis: | The consequence of direct exposure to HO. radical (chemically generated by Fenton's reaction) of partially purified rat liver PKC has been evaluated in this work. PKC inhibited Fenton-dependent HO. generation, probably due to the binding of copper ions to the enzyme. PKC activity was inhibited by H2O2. Copper ions were able to increase the H2O2-mediated damage to the enzyme, but only beyond a concentration threshold. The possible interactions between PKC and Fenton's reagents, in particular copper ions, is discussed. |
| Databáze: | OpenAIRE |
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